Ishrat Jahan Saifi
Aligarh Muslim University, India
Title: Glycation of serum albumin: Cause remarkable alteration in protein structure, immunogenicity and generation of early glycation end products
Biography
Biography: Ishrat Jahan Saifi
Abstract
Existing literature and research on diabetes mellitus describe that glycation of protein is very important as well as a harmful process, which may lead to development of DM in human body. Human serum albumin (HSA) is the most abundant protein in blood and it is highly prone to glycation by the reducing sugars. 2-deoxy d-Ribose (dRib) is a highly reactive reducing sugar which is produced in cells as a product of the enzyme thymidine phosphorylase. It is generated during the degradation of DNA in human body. It may cause glycation in HSA rapidly and it is involved in the development of DM. In present study, HSA was glycated with different concentrations of 2-deoxy d-ribose at 37ºC for 4 hours. UV spectroscopy, fluorescence spectroscopy and circular dichroism (CD) techniques have been done to determine the structural changes in HSA upon glycation. To check the immunogenicity of modified HSA, rabbits were immunized with native and dRib modified HSA individually. Modified HSA immune sera, show higher antibody titer as compare to pre-immune sera and also with the immune sera from the native HSA immunized rabbits. Results of this study suggested that dRib is the potential glycating agent that can cause alteration in protein structure. With the results of immunological study we can conclude that dRib modified HSA is more immunogenic than native HSA.
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